ID   AOX2_ARATH              Reviewed;         353 AA.
AC   O22049; Q4PS98;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   10-AUG-2010, entry version 85.
DE   RecName: Full=Alternative oxidase 2, mitochondrial;
DE            EC=1.-.-.-;
DE   Flags: Precursor;
GN   Name=AOX2; OrderedLocusNames=At5g64210; ORFNames=MSJ1.5;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; malvids; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Columbia; TISSUE=Leaf, and Stem;
RX   MEDLINE=98009993; PubMed=9349280; DOI=10.1023/A:1005818507743;
RA   Saisho D., Nambara E., Naito S., Tsutsumi N., Hirai A., Nakazono M.;
RT   "Characterization of the gene family for alternative oxidase from
RT   Arabidopsis thaliana.";
RL   Plant Mol. Biol. 35:585-596(1997).
RN   [2]
RP   SEQUENCE REVISION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND INDUCTION.
RX   MEDLINE=21327317; PubMed=11434463; DOI=10.1266/ggs.76.89;
RA   Saisho D., Nakazono M., Lee K.-H., Tsutsumi N., Akita S., Hirai A.;
RT   "The gene for alternative oxidase-2 (AOX2) from Arabidopsis thaliana
RT   consists of five exons unlike other AOX genes and is transcribed at an
RT   early stage during germination.";
RL   Genes Genet. Syst. 76:89-97(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=98162728; PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA   Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. III.
RT   Sequence features of the regions of 1,191,918 bp covered by seventeen
RT   physically assigned P1 clones.";
RL   DNA Res. 4:401-414(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA   Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   IRON-BINDING SITES.
RX   MEDLINE=99239925; PubMed=10225419; DOI=10.1016/S0014-5793(99)00376-2;
RA   Andersson M.E., Nordlund P.;
RT   "A revised model of the active site of alternative oxidase.";
RL   FEBS Lett. 449:17-22(1999).
CC   -!- FUNCTION: Catalyzes cyanide-resistant oxygen consumption. May
CC       increase respiration when the cytochrome respiratory pathway is
CC       restricted, or in response to low temperatures (By similarity).
CC   -!- COFACTOR: Binds 2 iron ions per subunit.
CC   -!- SUBUNIT: Homodimer; disulfide-linked (Probable).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC       membrane protein (Probable). Note=Mitochondrial, possibly in the
CC       inner surface of the inner mitochondrial membrane.
CC   -!- TISSUE SPECIFICITY: Maximally expressed in dry seeds.
CC   -!- DEVELOPMENTAL STAGE: Found predominantly during early stages of
CC       germination with maximum level at 12 hours after imbibition.
CC   -!- INDUCTION: Antimycin A has no effect on expression.
CC   -!- SIMILARITY: Belongs to the alternative oxidase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB09852.1; Type=Erroneous gene model prediction;
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DR   EMBL; AB003176; BAA22636.2; -; Genomic_DNA.
DR   EMBL; AB008268; BAB09852.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; DQ056738; AAY78882.1; -; mRNA.
DR   IPI; IPI00542540; -.
DR   RefSeq; NP_201226.2; -.
DR   UniGene; At.55697; -.
DR   STRING; O22049; -.
DR   PRIDE; O22049; -.
DR   EnsemblPlants; AT5G64210.1-TAIR; AT5G64210.1-P; AT5G64210-TAIR-G.
DR   GeneID; 836542; -.
DR   GenomeReviews; BA000015_GR; AT5G64210.
DR   KEGG; ath:AT5G64210; -.
DR   NMPDR; fig|3702.1.peg.28479; -.
DR   GeneFarm; 1754; 131.
DR   TAIR; At5g64210; -.
DR   eggNOG; euNOG04325; -.
DR   HOGENOM; HBG597538; -.
DR   InParanoid; O22049; -.
DR   ArrayExpress; O22049; -.
DR   Genevestigator; O22049; -.
DR   GermOnline; AT5G64210; Arabidopsis thaliana.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0007585; P:respiratory gaseous exchange; IEA:InterPro.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002680; AOX.
DR   Pfam; PF01786; AOX; 1.
DR   PIRSF; PIRSF005229; AOX; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Disulfide bond; Electron transport; Iron; Membrane;
KW   Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW   Oxidoreductase; Respiratory chain; Transit peptide; Transmembrane;
KW   Transmembrane helix; Transport.
FT   TRANSIT       1     21       Mitochondrion (Potential).
FT   CHAIN        22    353       Alternative oxidase 2, mitochondrial.
FT                                /FTId=PRO_0000001734.
FT   TRANSMEM    178    198       Helical; (Potential).
FT   TRANSMEM    240    260       Helical; (Potential).
FT   METAL       182    182       Iron (Potential).
FT   METAL       221    221       Iron (Potential).
FT   METAL       224    224       Iron (Potential).
FT   METAL       273    273       Iron (Potential).
FT   METAL       323    323       Iron (Potential).
FT   METAL       326    326       Iron (Potential).
FT   DISULFID    126    126       Interchain (Potential).
SQ   SEQUENCE   353 AA;  40087 MW;  DF7ACB113E57A133 CRC64;
     MSQLITKAAL RVLLVCGRGN CNMFVSSVSS TSVMKSPYEI TAPMRIHDWC GGFGDFKIGS
     KHVQGNFNLR WMGMSSASAM EKKDENLTVK KGQNGGGSVA VPSYWGIETA KMKITRKDGS
     DWPWNCFMPW ETYQANLSID LKKHHVPKNI ADKVAYRIVK LLRIPTDIFF QRRYGCRAMM
     LETVAAVPGM VGGMLLHLKS IRKFEHSGGW IKALLEEAEN ERMHLMTMME LVKPKWYERL
     LVMLVQGIFF NSFFVCYVIS PRLAHRVVGY LEEEAIHSYT EFLKDIDNGK IENVAAPAIA
     IDYWRLPKDA TLKDVVTVIR ADEAHHRDVN HFASDIRNQG KELREAAAPI GYH
//